ArticleThe Journal of biological chemistry2011
Polar transmembrane-based amino acids in presenilin 1 are involved in endoplasmic reticulum localization, Pen2 protein binding, and γ-secretase complex stabilization.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- The role of ladderlectin in spermatogenesis and ovarian sperm storage in the black rockfish (Sebastes schlegelii).Communications biology · 2025Article
- SARS-CoV-2 spike host cell surface exposure promoted by a COPI sorting inhibitor.Acta pharmaceutica Sinica. B · 2023Article
- A disease causing ATLASTIN 3 mutation affects multiple endoplasmic reticulum-related pathways.Cellular and molecular life sciences : CMLS · 2019Article
- G206D Mutation of Presenilin-1 Reduces Pen2 Interaction, Increases Aβ42/Aβ40 Ratio and Elevates ER Ca(2+) Accumulation.Molecular neurobiology · 2015Article
- Gamma-secretase subunits associate in intracellular membrane compartments in Arabidopsis thaliana.Journal of experimental botany · 2014Article
- Mutant ELOVL4 that causes autosomal dominant stargardt-3 macular dystrophy is misrouted to rod outer segment disks.Investigative ophthalmology & visual science · 2014Article
- The very many faces of presenilins and the γ-secretase complex.Protoplasma · 2013Review
- Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer's disease.Alzheimer's research & therapy · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
γ-Secretase is composed of the four membrane proteins presenilin, nicastrin, Pen2, and Aph1. These four proteins assemble in a coordinated and regulated manner into a high molecular weight complex. The subunits constitute a total of 19 transmembrane domains (TMD), with many carrying important amino acids involved in catalytic activity, interaction with other subunits, or in ER retention/retrieval of unassembled subunits. We here focus on TMD4 of presenilin 1 (PS1) and show that a number of polar amino acids are critical for γ-secretase assembly and function. An asparagine, a threonine, and an aspartate form a polar interface important for endoplasmic reticulum retention/retrieval. A single asparagine in TMD4 of PS1 is involved in a protein-protein interaction by binding to another asparagine in Pen2. Intriguingly, a charged aspartate in TMD4 is critical for γ-secretase activity, most likely by stabilizing the newly formed complex.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.